A commentary is offered on the spectroscopic way to characterize axial amine-iron ligation in a heme protein. This is of use to determine whether a lysine replaces the methionine ligand in the alkaline form of c-type cytochromes.

Characterization of Mutant Met100Lys of Cytochrome c-550 from Thiobacillus versutus with Lysine-Histidine Heme Ligation / Sola, Marco. - In: CHEMTRACTS. INORGANIC CHEMISTRY. - ISSN 1051-7227. - STAMPA. - 6:(1994), pp. 125-131.

Characterization of Mutant Met100Lys of Cytochrome c-550 from Thiobacillus versutus with Lysine-Histidine Heme Ligation.

SOLA, Marco
1994

Abstract

A commentary is offered on the spectroscopic way to characterize axial amine-iron ligation in a heme protein. This is of use to determine whether a lysine replaces the methionine ligand in the alkaline form of c-type cytochromes.
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131
Characterization of Mutant Met100Lys of Cytochrome c-550 from Thiobacillus versutus with Lysine-Histidine Heme Ligation / Sola, Marco. - In: CHEMTRACTS. INORGANIC CHEMISTRY. - ISSN 1051-7227. - STAMPA. - 6:(1994), pp. 125-131.
Sola, Marco
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11380/21647
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